(data stored in ACNUC7421 zone)

SWISSPROT: BOFA_BACSU

ID   BOFA_BACSU              Reviewed;          87 AA.
AC   P24282;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=Sigma-K factor-processing regulatory protein BofA;
DE   AltName: Full=Bypass-of-forespore protein A;
GN   Name=bofA; OrderedLocusNames=BSU00230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=2124672; DOI=10.1093/nar/18.23.6771;
RA   Alonso J.C., Shirahige K., Ogasawara N.;
RT   "Molecular cloning, genetic characterization and DNA sequence analysis of
RT   the recM region of Bacillus subtilis.";
RL   Nucleic Acids Res. 18:6771-6777(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 55.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=1577688; DOI=10.1128/jb.174.10.3177-3184.1992;
RA   Ricca E., Cutting S.M., Losick R.;
RT   "Characterization of bofA, a gene involved in intercompartmental regulation
RT   of pro-sigma K processing during sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 174:3177-3184(1992).
RN   [6]
RP   TOPOLOGY.
RX   PubMed=9141672; DOI=10.1099/00221287-143-4-1053;
RA   Varcamonti M., Marasco R., de Felice M., Sacco M.;
RT   "Membrane topology analysis of the Bacillus subtilis BofA protein involved
RT   in pro-sigma K processing.";
RL   Microbiology 143:1053-1058(1997).
RN   [7]
RP   FUNCTION IN STABILIZING SPOIVFA.
RX   PubMed=10464210;
RA   Resnekov O.;
RT   "Role of the sporulation protein BofA in regulating activation of the
RT   Bacillus subtilis developmental transcription factor sigmaK.";
RL   J. Bacteriol. 181:5384-5388(1999).
RN   [8]
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=11959848; DOI=10.1101/gad.977702;
RA   Rudner D.Z., Losick R.;
RT   "A sporulation membrane protein tethers the pro-sigmaK processing enzyme to
RT   its inhibitor and dictates its subcellular localization.";
RL   Genes Dev. 16:1007-1018(2002).
RN   [9]
RP   FUNCTION.
RX   PubMed=15087499; DOI=10.1073/pnas.0307709101;
RA   Zhou R., Kroos L.;
RT   "BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an
RT   intercompartmental signaling pathway during Bacillus subtilis
RT   sporulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6385-6390(2004).
CC   -!- FUNCTION: Involved in the mediation of the intercompartmental coupling
CC       of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB-
CC       processing activity until a signal has been received from the
CC       forespore. Could inhibit SpoIVFB metalloprotease activity by
CC       coordinating a zinc in the SpoIVFB active site, preventing access of a
CC       water molecule and the sequence of pro-sigma K, which are necessary for
CC       peptide bond hydrolysis to produce sigma-K.
CC       {ECO:0000269|PubMed:10464210, ECO:0000269|PubMed:11959848,
CC       ECO:0000269|PubMed:15087499}.
CC   -!- SUBUNIT: Forms a complex with SpoIVFA and SpoIVFB localized in the
CC       mother cell membrane surrounding the forespore.
CC       {ECO:0000269|PubMed:11959848}.
CC   -!- SUBCELLULAR LOCATION: Forespore outer membrane; Multi-pass membrane
CC       protein.
DR   EMBL; X17014; CAA34880.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05259.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11799.2; -; Genomic_DNA.
DR   PIR; B41869; B41869.
DR   RefSeq; NP_387904.2; NC_000964.3.
DR   RefSeq; WP_003225421.1; NZ_JNCM01000024.1.
DR   STRING; 224308.BSU00230; -.
DR   PaxDb; P24282; -.
DR   EnsemblBacteria; CAB11799; CAB11799; BSU00230.
DR   GeneID; 937025; -.
DR   KEGG; bsu:BSU00230; -.
DR   PATRIC; fig|224308.179.peg.23; -.
DR   eggNOG; ENOG41067KS; Bacteria.
DR   eggNOG; ENOG41128H6; LUCA.
DR   HOGENOM; HOG000060841; -.
DR   KO; K06317; -.
DR   OMA; LLYILGW; -.
DR   BioCyc; BSUB:BSU00230-MONOMER; -.
DR   PRO; PR:P24282; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR010001; BofA.
DR   Pfam; PF07441; BofA; 1.
DR   TIGRFAMs; TIGR02862; spore_BofA; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P24282.
DR   SWISS-2DPAGE; P24282.
KW   Membrane; Metal-binding; Reference proteome; Sporulation; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..87
FT                   /note="Sigma-K factor-processing regulatory protein BofA"
FT                   /id="PRO_0000064969"
FT   TOPO_DOM        1..2
FT                   /note="Forespore intermembrane space"
FT                   /evidence="ECO:0000305|PubMed:9141672"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        24..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:9141672"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        58..87
FT                   /note="Forespore intermembrane space"
FT                   /evidence="ECO:0000305|PubMed:9141672"
FT   METAL           57
FT                   /note="Zinc; shared with SpoIVFB"
FT   CONFLICT        55
FT                   /note="G -> C (in Ref. 1; CAA34880 and 2; BAA05259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   87 AA;  8964 MW;  F9B1CB8E6826B70E CRC64;
     MEPIFIIGII LGLVILLFLS GSAAKPLKWI GITAVKFVAG ALLLVCVNMF GGSLGIHVPI
     NLVTTAISGI LGIPGIAALV VIKQFII
//

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